PT1347730E - Anticorpos anti-cd30 recombinantes e suas utilizações - Google Patents
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- PT1347730E PT1347730E PT01986050T PT01986050T PT1347730E PT 1347730 E PT1347730 E PT 1347730E PT 01986050 T PT01986050 T PT 01986050T PT 01986050 T PT01986050 T PT 01986050T PT 1347730 E PT1347730 E PT 1347730E
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Classifications
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- C07K16/18—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans
- C07K16/28—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans against receptors, cell surface antigens or cell surface determinants
- C07K16/2878—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans against receptors, cell surface antigens or cell surface determinants against the NGF-receptor/TNF-receptor superfamily, e.g. CD27, CD30, CD40, CD95
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- A61K47/50—Medicinal preparations characterised by the non-active ingredients used, e.g. carriers or inert additives; Targeting or modifying agents chemically bound to the active ingredient the non-active ingredient being chemically bound to the active ingredient, e.g. polymer-drug conjugates
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- A61K47/68—Medicinal preparations characterised by the non-active ingredients used, e.g. carriers or inert additives; Targeting or modifying agents chemically bound to the active ingredient the non-active ingredient being chemically bound to the active ingredient, e.g. polymer-drug conjugates the non-active ingredient being a modifying agent the modifying agent being an antibody, an immunoglobulin or a fragment thereof, e.g. an Fc-fragment
- A61K47/6835—Medicinal preparations characterised by the non-active ingredients used, e.g. carriers or inert additives; Targeting or modifying agents chemically bound to the active ingredient the non-active ingredient being chemically bound to the active ingredient, e.g. polymer-drug conjugates the non-active ingredient being a modifying agent the modifying agent being an antibody, an immunoglobulin or a fragment thereof, e.g. an Fc-fragment the modifying agent being an antibody or an immunoglobulin bearing at least one antigen-binding site
- A61K47/6849—Medicinal preparations characterised by the non-active ingredients used, e.g. carriers or inert additives; Targeting or modifying agents chemically bound to the active ingredient the non-active ingredient being chemically bound to the active ingredient, e.g. polymer-drug conjugates the non-active ingredient being a modifying agent the modifying agent being an antibody, an immunoglobulin or a fragment thereof, e.g. an Fc-fragment the modifying agent being an antibody or an immunoglobulin bearing at least one antigen-binding site the antibody targeting a receptor, a cell surface antigen or a cell surface determinant
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Landscapes
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- Preparation Of Compounds By Using Micro-Organisms (AREA)
- Micro-Organisms Or Cultivation Processes Thereof (AREA)
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Families Citing this family (131)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US7090843B1 (en) † | 2000-11-28 | 2006-08-15 | Seattle Genetics, Inc. | Recombinant anti-CD30 antibodies and uses thereof |
| US20040018194A1 (en) * | 2000-11-28 | 2004-01-29 | Francisco Joseph A. | Recombinant anti-CD30 antibodies and uses thereof |
| US20110313230A1 (en) | 2001-05-11 | 2011-12-22 | Terrance Grant Johns | Specific binding proteins and uses thereof |
| WO2003043583A2 (en) * | 2001-11-20 | 2003-05-30 | Seattle Genetics, Inc. | Treatment of immunological disorders using anti-cd30 antibodies |
| JP2005517674A (ja) * | 2002-01-03 | 2005-06-16 | フラームス・インテルウニフェルシタイル・インステイチュート・フォール・ビオテヒノロヒー・ヴェーゼットウェー | 腫瘍の処置に有用な新規免疫コンジュゲート |
| WO2003059282A2 (en) * | 2002-01-09 | 2003-07-24 | Medarex, Inc. | Human monoclonal antibodies against cd30 |
| US20070148171A1 (en) * | 2002-09-27 | 2007-06-28 | Xencor, Inc. | Optimized anti-CD30 antibodies |
| CA2802205C (en) * | 2002-07-31 | 2016-01-19 | Seattle Genetics, Inc. | Drug conjugates and their use for treating cancer, an autoimmune disease or an infectious disease |
| NZ583292A (en) | 2003-11-06 | 2012-03-30 | Seattle Genetics Inc | Monomethylvaline compounds capable of conjugation to ligands |
| KR20070083899A (ko) | 2004-10-01 | 2007-08-24 | 메다렉스, 인코포레이티드 | Ｃｄ30 양성 림프종의 치료 방법 |
| BRPI0607203A2 (pt) | 2005-02-18 | 2009-08-25 | Medarex Inc | anticorpo anti-cd30 isolado, célula hospedeira, métodos para inibir o crescimento de células cd30+, e, uso de um anticorpo anti-cd30 desfucosilado |
| CA2625998C (en) * | 2005-10-06 | 2015-12-01 | Xencor, Inc. | Optimized anti-cd30 antibodies |
| WO2008025020A2 (en) * | 2006-08-25 | 2008-02-28 | Seattle Genetics, Inc. | Cd30 binding agents and uses thereof |
| MY150531A (en) | 2007-07-16 | 2014-01-30 | Genentech Inc | Anti-cd79b antibodies and immunoconjugates and methods of use |
| RU2557319C2 (ru) | 2007-07-16 | 2015-07-20 | Дженентек, Инк. | ГУМАНИЗИРОВАННЫЕ АНТИТЕЛА ПРОТИВ CD79b И ИММУНОКОНЪЮГАТЫ И СПОСОБЫ ПРИМЕНЕНИЯ |
| EP2185188B1 (en) | 2007-08-22 | 2014-08-06 | Medarex, L.L.C. | Site-specific attachment of drugs or other agents to engineered antibodies with c-terminal extensions |
| AU2008310908B2 (en) | 2007-10-12 | 2014-01-09 | Seagen Inc. | Combination therapy with antibody-drug conjugates |
| DK2657253T3 (en) | 2008-01-31 | 2017-10-09 | Genentech Inc | Anti-CD79b antibodies and immune conjugates and methods of use |
| EP2727606A3 (en) | 2008-09-08 | 2015-09-23 | Psma Development Company, L.L.C. | Compounds for killing psma-expressing, taxane-resistant cancer cells |
| CA3150199C (en) | 2009-01-09 | 2025-07-22 | Seagen Inc | WEEKLY DOSING REGIMEN FOR ANTI-CD30 ANTIBODY CONJUGATIONS VC-PAB-MMAE - MEDICINE |
| KR101224468B1 (ko) * | 2009-05-20 | 2013-01-23 | 주식회사 파멥신 | 신규한 형태의 이중표적항체 및 그 용도 |
| US20110076232A1 (en) | 2009-09-29 | 2011-03-31 | Ludwig Institute For Cancer Research | Specific binding proteins and uses thereof |
| ES3004351T3 (en) | 2010-10-22 | 2025-03-12 | Seagen Inc | Synergistic effects between auristatin-based antibody drug conjugates and inhibitors of the pi3k-akt mtor pathway |
| WO2013092998A1 (en) | 2011-12-23 | 2013-06-27 | Innate Pharma | Enzymatic conjugation of antibodies |
| PT2841456T (pt) * | 2012-04-27 | 2018-10-19 | Novo Nordisk As | Proteinas de ligação ao antigénio do ligando de cd30 humano |
| WO2014009426A2 (en) | 2012-07-13 | 2014-01-16 | Innate Pharma | Screening of conjugated antibodies |
| KR102498405B1 (ko) | 2012-10-11 | 2023-02-09 | 다이이찌 산쿄 가부시키가이샤 | 글리신아미드 화합물의 제조 방법 |
| WO2014061277A1 (ja) | 2012-10-19 | 2014-04-24 | 第一三共株式会社 | 親水性構造を含むリンカーで結合させた抗体－薬物コンジュゲート |
| WO2014072482A1 (en) | 2012-11-09 | 2014-05-15 | Innate Pharma | Recognition tags for tgase-mediated conjugation |
| EP2922818B1 (en) | 2012-11-24 | 2018-09-05 | Hangzhou Dac Biotech Co., Ltd | Hydrophilic linkers and their uses for conjugation of drugs to cell binding molecules |
| US9353150B2 (en) | 2012-12-04 | 2016-05-31 | Massachusetts Institute Of Technology | Substituted pyrazino[1′,2′:1 ,5]pyrrolo[2,3-b]-indole-1,4-diones for cancer treatment |
| US9089614B2 (en) | 2012-12-21 | 2015-07-28 | Bioalliance C.V. | Hydrophilic self-immolative linkers and conjugates thereof |
| WO2014152199A1 (en) | 2013-03-15 | 2014-09-25 | Abbvie Inc. | Antibody drug conjugate (adc) purification |
| HRP20190672T1 (hr) | 2013-03-15 | 2019-08-23 | AbbVie Deutschland GmbH & Co. KG | Konjugirane formulacije anti-egfr protutijelo-lijek |
| WO2014140300A1 (en) | 2013-03-15 | 2014-09-18 | Innate Pharma | Solid phase tgase-mediated conjugation of antibodies |
| JP6433085B2 (ja) | 2013-04-09 | 2018-12-05 | ボストン バイオメディカル， インコーポレイテッド | がんの処置に使用するための２−アセチルナフト［２，３−ｂ］フラン−４，９−ジオン |
| WO2014202773A1 (en) | 2013-06-20 | 2014-12-24 | Innate Pharma | Enzymatic conjugation of polypeptides |
| KR20160042871A (ko) | 2013-06-21 | 2016-04-20 | 이나뜨 파르마, 에스.아. | 폴리펩티드의 효소적 콘쥬게이션 |
| BR112016007622A2 (pt) | 2013-10-15 | 2018-01-23 | Seattle Genetics, Inc. | composto, composição farmacêutica, conjugado de ligante-droga, e, método para tratar câncer |
| AU2015210578B2 (en) | 2014-01-29 | 2020-04-16 | Jiangsu Hengrui Medicine Co., Ltd. | Ligand-cytotoxic drug conjugate, preparation method therefor, and uses thereof |
| AU2014384434B2 (en) | 2014-02-28 | 2016-11-03 | Hangzhou Dac Biotech Co., Ltd | Charged linkers and their uses for conjugation |
| WO2015142675A2 (en) | 2014-03-15 | 2015-09-24 | Novartis Ag | Treatment of cancer using chimeric antigen receptor |
| JP2017528418A (ja) | 2014-06-20 | 2017-09-28 | バイオアライアンス コマンディテール フェンノートシャップ | 抗葉酸受容体アルファ（ｆｒａ）抗体−薬物コンジュゲート及びその使用方法 |
| AU2015282627B2 (en) | 2014-06-30 | 2020-04-02 | Glykos Finland Oy | Saccharide derivative of a toxic payload and antibody conjugates thereof |
| JP2017528433A (ja) | 2014-07-21 | 2017-09-28 | ノバルティス アーゲー | 低い免疫増強用量のｍＴＯＲ阻害剤とＣＡＲの組み合わせ |
| DK3262071T3 (da) | 2014-09-23 | 2020-06-15 | Hoffmann La Roche | Fremgangsmåde til anvendelse af anti-CD79b-immunkonjugater |
| WO2016126608A1 (en) | 2015-02-02 | 2016-08-11 | Novartis Ag | Car-expressing cells against multiple tumor antigens and uses thereof |
| WO2016172583A1 (en) | 2015-04-23 | 2016-10-27 | Novartis Ag | Treatment of cancer using chimeric antigen receptor and protein kinase a blocker |
| MX2017015493A (es) | 2015-05-30 | 2018-02-09 | Molecular Templates Inc | Andamiajes de la subunidad a de la toxina shiga desinmunizados y moleculas con direccion a las celulas que los comprenden. |
| EA201792623A1 (ru) | 2015-06-03 | 2018-04-30 | Бостон Биомедикал, Инк. | Композиции, содержащие ингибитор стволовости рака и иммунотерапевтический агент, для применения в лечении рака |
| WO2015151078A2 (en) | 2015-06-15 | 2015-10-08 | Suzhou M-Conj Biotech Co., Ltd | Hydrophilic linkers for conjugation |
| NZ739830A (en) | 2015-07-12 | 2021-12-24 | Hangzhou Dac Biotech Co Ltd | Bridge linkers for conjugation of cell-binding molecules |
| US9839687B2 (en) | 2015-07-15 | 2017-12-12 | Suzhou M-Conj Biotech Co., Ltd. | Acetylenedicarboxyl linkers and their uses in specific conjugation of a cell-binding molecule |
| WO2017027392A1 (en) | 2015-08-07 | 2017-02-16 | Novartis Ag | Treatment of cancer using chimeric cd3 receptor proteins |
| CN108603200B (zh) | 2015-11-23 | 2022-08-19 | 诺华股份有限公司 | 优化的慢病毒转移载体及其用途 |
| JP2019500394A (ja) | 2015-12-30 | 2019-01-10 | ノバルティス アーゲー | 有効性が増強された免疫エフェクター細胞治療 |
| ES2880731T3 (es) | 2016-01-08 | 2021-11-25 | Altrubio Inc | Anticuerpos anti-PSGL-1 tetravalentes y usos de los mismos |
| EP3432924A1 (en) | 2016-03-23 | 2019-01-30 | Novartis AG | Cell secreted minibodies and uses thereof |
| BR112018069273A2 (pt) | 2016-03-25 | 2019-01-22 | Seattle Genetics Inc | métodos para preparação de um composto e para tratamento de um indivíduo com uma malignidade hematológica, composto, composição, e, intermediário ligante de fármaco ou composto ligante de fármaco |
| WO2017197045A1 (en) | 2016-05-11 | 2017-11-16 | Movassaghi Mohammad | Convergent and enantioselective total synthesis of communesin analogs |
| JP7523907B2 (ja) | 2016-11-14 | 2024-07-29 | 武田薬品工業株式会社 | 非成人のヒトに対する抗ｃｄ３０抗体－薬物コンジュゲートの投与 |
| KR102345175B1 (ko) | 2016-11-14 | 2021-12-31 | 항저우 디에이씨 바이오테크 씨오, 엘티디 | 결합 링커, 그러한 결합 링커를 함유하는 세포 결합 분자-약물 결합체, 링커를 갖는 그러한 결합체의 제조 및 사용 |
| US11299469B2 (en) | 2016-11-29 | 2022-04-12 | Sumitomo Dainippon Pharma Oncology, Inc. | Naphthofuran derivatives, preparation, and methods of use thereof |
| WO2018111340A1 (en) | 2016-12-16 | 2018-06-21 | Novartis Ag | Methods for determining potency and proliferative function of chimeric antigen receptor (car)-t cells |
| CN106854245A (zh) * | 2016-12-28 | 2017-06-16 | 无锡傲锐东源生物科技有限公司 | 抗cd30蛋白单克隆抗体及其用途 |
| EP4043485A1 (en) | 2017-01-26 | 2022-08-17 | Novartis AG | Cd28 compositions and methods for chimeric antigen receptor therapy |
| WO2018144535A1 (en) | 2017-01-31 | 2018-08-09 | Novartis Ag | Treatment of cancer using chimeric t cell receptor proteins having multiple specificities |
| US20200048359A1 (en) | 2017-02-28 | 2020-02-13 | Novartis Ag | Shp inhibitor compositions and uses for chimeric antigen receptor therapy |
| WO2018158716A1 (en) | 2017-03-02 | 2018-09-07 | Cadila Healthcare Limited | Novel protein drug conjugate formulation |
| US11730822B2 (en) | 2017-03-24 | 2023-08-22 | Seagen Inc. | Process for the preparation of glucuronide drug-linkers and intermediates thereof |
| WO2018213424A1 (en) | 2017-05-17 | 2018-11-22 | Boston Biomedical, Inc. | Methods for treating cancer |
| WO2018229715A1 (en) | 2017-06-16 | 2018-12-20 | Novartis Ag | Compositions comprising anti-cd32b antibodies and methods of use thereof |
| MX2020003664A (es) | 2017-10-11 | 2020-10-12 | Seattle Genetics Inc | Metodos de reduccion de efectos secundarios del tratamiento con conjugado anticuerpo anti-cd30-farmaco. |
| US10640508B2 (en) | 2017-10-13 | 2020-05-05 | Massachusetts Institute Of Technology | Diazene directed modular synthesis of compounds with quaternary carbon centers |
| MX2020004229A (es) | 2017-10-25 | 2020-07-22 | Novartis Ag | Metodos de produccion de celulas que expresan receptores antigenicos quimericos. |
| US20210040205A1 (en) | 2017-10-25 | 2021-02-11 | Novartis Ag | Antibodies targeting cd32b and methods of use thereof |
| US20210179709A1 (en) | 2017-10-31 | 2021-06-17 | Novartis Ag | Anti-car compositions and methods |
| MX2020004563A (es) | 2017-11-01 | 2020-08-13 | Seattle Genetics Inc | Metodos de reduccion de efectos secundarios del tratamiento con conjugado anticuerpo anti-cd30-farmaco. |
| CN117003874A (zh) | 2018-03-20 | 2023-11-07 | 鸿运华宁（杭州）生物医药有限公司 | Gipr抗体及其与glp-1的融合蛋白质，以及其药物组合物和应用 |
| SG11202009264WA (en) | 2018-03-23 | 2020-10-29 | Seattle Genetics Inc | Use of antibody drug conjugates comprising tubulin disrupting agents to treat solid tumor |
| US20210047405A1 (en) | 2018-04-27 | 2021-02-18 | Novartis Ag | Car t cell therapies with enhanced efficacy |
| US20210396739A1 (en) | 2018-05-01 | 2021-12-23 | Novartis Ag | Biomarkers for evaluating car-t cells to predict clinical outcome |
| US20210213063A1 (en) | 2018-05-25 | 2021-07-15 | Novartis Ag | Combination therapy with chimeric antigen receptor (car) therapies |
| TW202519270A (zh) | 2018-06-07 | 2025-05-16 | 美商思進公司 | 喜樹鹼結合物 |
| WO2019237035A1 (en) | 2018-06-08 | 2019-12-12 | Intellia Therapeutics, Inc. | Compositions and methods for immunooncology |
| AR116109A1 (es) | 2018-07-10 | 2021-03-31 | Novartis Ag | Derivados de 3-(5-amino-1-oxoisoindolin-2-il)piperidina-2,6-diona y usos de los mismos |
| EP3856777A1 (en) | 2018-09-24 | 2021-08-04 | The Medical College of Wisconsin, Inc. | Anti-cd30 antibodies and methods of use |
| CN118806924A (zh) | 2018-09-26 | 2024-10-22 | 江苏恒瑞医药股份有限公司 | 依喜替康类似物的配体-药物偶联物及其制备方法和应用 |
| CN113613678A (zh) | 2018-10-01 | 2021-11-05 | 西进公司 | 使用抗cd30抗体药物缀合物疗法治疗外周t细胞淋巴瘤的方法 |
| US20220016277A1 (en) | 2018-11-20 | 2022-01-20 | Cornell University | Macrocyclic complexes of radionuclides and their use in radiotherapy of cancer |
| WO2020128972A1 (en) | 2018-12-20 | 2020-06-25 | Novartis Ag | Dosing regimen and pharmaceutical combination comprising 3-(1-oxoisoindolin-2-yl)piperidine-2,6-dione derivatives |
| ES2982474T3 (es) | 2019-02-15 | 2024-10-16 | Novartis Ag | Derivados de 3-(1-oxoisoindolin-2-il)piperidin-1,6-diona sustituidos y usos de estos |
| ES3032659T3 (en) | 2019-02-15 | 2025-07-23 | Novartis Ag | 3-(1-oxo-5-(piperidin-4-yl)isoindolin-2-yl)piperidine-2,6-dione derivatives and uses thereof |
| US20220160771A1 (en) | 2019-04-10 | 2022-05-26 | Iulia Diaconu | Flt3-specific chimeric antigen receptors and methods of using the same |
| EP4032892A4 (en) | 2019-09-18 | 2023-10-18 | Baili-Bio (Chengdu) Pharmaceutical Co., Ltd. | CAMPTOTHECIN DERIVATIVE AND CONJUGATE THEREOF |
| KR20220069964A (ko) | 2019-09-25 | 2022-05-27 | 씨젠 인크. | 조혈암의 치료를 위한 항-cd30 adc, 항-pd-1 및 화학치료제 조합 |
| CA3152316A1 (en) | 2019-10-04 | 2021-04-08 | Scott C. Jeffrey | Camptothecin peptide conjugates |
| WO2021067820A1 (en) | 2019-10-04 | 2021-04-08 | Seagen Inc. | Formulation of antibody-drug conjugate |
| CN115397472A (zh) | 2019-11-04 | 2022-11-25 | 思进股份有限公司 | 抗cd30抗体-药物缀合物及其用于治疗hiv感染的用途 |
| MX2022007759A (es) | 2019-12-20 | 2022-07-19 | Novartis Ag | Combinacion del anticuerpo anti tim-3 mbg453 y anticuerpo anti tgf-beta nis793, con o sin decitabina o el anticuerpo anti pd-1 spartalizumab, para el tratamiento de mielofibrosis y sindrome mielodisplasico. |
| WO2021148003A1 (zh) | 2020-01-22 | 2021-07-29 | 上海森辉医药有限公司 | 艾日布林衍生物的药物偶联物、其制备方法及其在医药上的应用 |
| JP2023512084A (ja) | 2020-01-31 | 2023-03-23 | シージェン インコーポレイテッド | 抗ｃｄ３０抗体薬物コンジュゲート及び非ホジキンリンパ腫の治療のためのその使用 |
| MX2022011770A (es) | 2020-03-25 | 2022-10-18 | Jiangsu Hengrui Pharmaceuticals Co Ltd | Composicion farmaceutica que contiene un conjugado de anticuerpo-farmaco y uso de la misma. |
| CN115103858B (zh) | 2020-03-25 | 2025-07-15 | 江苏恒瑞医药股份有限公司 | 一种抗体药物偶联物的制备方法 |
| US20230173093A1 (en) | 2020-04-10 | 2023-06-08 | Seagen Inc. | Charge variant linkers |
| IL298155A (en) | 2020-05-13 | 2023-01-01 | Seagen Inc | Methods of treating cancer using a combination of anti-cd30 antibody-drug conjugates |
| US20230332104A1 (en) | 2020-06-11 | 2023-10-19 | Novartis Ag | Zbtb32 inhibitors and uses thereof |
| MX2022015852A (es) | 2020-06-23 | 2023-01-24 | Novartis Ag | Regimen de dosificacion que comprende derivados de 3-(1-oxoisoindolin-2-il)piperidina-2,6-diona. |
| EP4188549A1 (en) | 2020-08-03 | 2023-06-07 | Novartis AG | Heteroaryl substituted 3-(1-oxoisoindolin-2-yl)piperidine-2,6-dione derivatives and uses thereof |
| TW202246242A (zh) | 2021-01-15 | 2022-12-01 | 美商西健公司 | 免疫調節抗體藥物結合物 |
| US12036286B2 (en) | 2021-03-18 | 2024-07-16 | Seagen Inc. | Selective drug release from internalized conjugates of biologically active compounds |
| TW202304979A (zh) | 2021-04-07 | 2023-02-01 | 瑞士商諾華公司 | 抗ＴＧＦβ抗體及其他治療劑用於治療增殖性疾病之用途 |
| MX2023012364A (es) | 2021-04-20 | 2023-11-01 | Seagen Inc | Modulacion de citotoxicidad celular dependiente de anticuerpos. |
| CN118056008A (zh) | 2021-04-27 | 2024-05-17 | 诺华股份有限公司 | 病毒载体生产系统 |
| WO2022251850A1 (en) | 2021-05-28 | 2022-12-01 | Seagen Inc. | Anthracycline antibody conjugates |
| MX2024005080A (es) | 2021-10-29 | 2024-05-13 | Seagen Inc | Metodos para tratar cancer con una combinacion de un anticuerpo anti-pd-1 y un conjugado de anticuerpo anti-cd30-farmaco. |
| CA3236930A1 (en) | 2021-11-03 | 2022-04-21 | Hangzhou Dac Biotech Co., Ltd. | Specific conjugation of an antibody |
| CN114891101B (zh) * | 2021-12-02 | 2023-06-16 | 吉林省农业科学院 | 一种牛肌肉生长抑制素蛋白单克隆抗体及其应用 |
| EP4493223A2 (en) | 2022-03-17 | 2025-01-22 | Seagen Inc. | Camptothecin conjugates |
| WO2023214325A1 (en) | 2022-05-05 | 2023-11-09 | Novartis Ag | Pyrazolopyrimidine derivatives and uses thereof as tet2 inhibitors |
| WO2023215740A1 (en) | 2022-05-06 | 2023-11-09 | Seagen Inc. | Immunomodulatory antibody-drug conjugates |
| WO2024085182A1 (ja) | 2022-10-18 | 2024-04-25 | Ｍｅｉｊｉ Ｓｅｉｋａファルマ株式会社 | Ｔ細胞性腫瘍の治療剤 |
| WO2024089639A1 (en) | 2022-10-26 | 2024-05-02 | Novartis Ag | Lentiviral formulations |
| EP4634227A1 (en) | 2022-12-13 | 2025-10-22 | Seagen Inc. | Site-specific engineered cysteine antibody drug conjugates |
| AR132178A1 (es) | 2023-03-22 | 2025-06-04 | Salubris Biotherapeutics Inc | Dominios de unión al antígeno anti-5t4, conjugados anticuerpo-fármaco, y métodos de uso de los mismos |
| WO2024243441A1 (en) | 2023-05-24 | 2024-11-28 | Kumquat Biosciences Inc. | Heterocyclic compounds and uses thereof |
| WO2025090774A1 (en) | 2023-10-24 | 2025-05-01 | Seagen Inc. | Chemotherapeutic compounds and methods of use |
| WO2025096626A1 (en) | 2023-10-31 | 2025-05-08 | Seagen Inc. | Methods of treating cancers using anti-cd30 antibody-drug conjugates |
| WO2025149947A1 (en) | 2024-01-12 | 2025-07-17 | Seagen Inc. | Antibody-drug conjugates |
| WO2025169056A1 (en) | 2024-02-06 | 2025-08-14 | Seagen Inc. | Methods of treating cancers using anti-cd30 antibody-drug conjugates |
| CN119331093B (zh) * | 2024-11-04 | 2025-07-11 | 武汉伊莱瑞特生物科技股份有限公司 | 一种抗CD30的兔源Fab抗体及其制备方法和应用 |
Family Cites Families (15)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US5165923A (en) * | 1989-11-20 | 1992-11-24 | Imperial Cancer Research Technology | Methods and compositions for the treatment of hodgkin's disease |
| WO1991007437A2 (en) | 1989-11-20 | 1991-05-30 | Parker, David, L. | Improved cd-30 antibodies and fragments thereof |
| DE4200043A1 (de) | 1991-11-11 | 1993-05-13 | Stein Harald Prof Dr | Lymphoides cd30-antigen (ki-1), dessen protein- und die zugehoerige nucleotidsequenz, seine herstellung sowie mittel zur diagnose und untersuchung von tumoren |
| WO1992022324A1 (en) | 1991-06-14 | 1992-12-23 | Xoma Corporation | Microbially-produced antibody fragments and their conjugates |
| WO1993024135A1 (en) | 1992-05-26 | 1993-12-09 | Immunex Corporation | Novel cytokine that binds cd30 |
| CA2146747C (en) | 1992-10-09 | 2006-12-19 | Brian A. Naughton | Liver reserve cells |
| WO1994015969A1 (fr) | 1993-01-14 | 1994-07-21 | Juridical Foundation The Chemo-Sero-Therapeutic Research Institute | Anticorps anti-vih recombine et sa preparation |
| ATE306930T1 (de) * | 1994-08-12 | 2005-11-15 | Immunomedics Inc | Für b-zell-lymphom und leukämiezellen spezifische immunkonjugate und humane antikörper |
| DE69605181T3 (de) * | 1995-01-18 | 2006-08-24 | Roche Diagnostics Gmbh | Antikörper gegen cd30, die proteolytische spaltung und abgabe des membrangebundenen cd30 antigens verhindern |
| DE19543039C1 (de) | 1995-11-08 | 1996-11-21 | Medac Klinische Spezialpraep | Rekombinante Liganden für das menschliche Zellmembran-Antigen CD30 |
| DE19640733A1 (de) * | 1996-10-02 | 1998-04-09 | Abken Hinrich | Verfahren zur Hemmung der unbegrenzten Profileration, Tumorbildung oder Metastasierung CD30 Antigen exprimierender Zellen |
| WO2001080880A2 (de) | 2000-04-22 | 2001-11-01 | Stefan Barth | Apoptotika |
| US20040018194A1 (en) | 2000-11-28 | 2004-01-29 | Francisco Joseph A. | Recombinant anti-CD30 antibodies and uses thereof |
| US7090843B1 (en) † | 2000-11-28 | 2006-08-15 | Seattle Genetics, Inc. | Recombinant anti-CD30 antibodies and uses thereof |
| WO2003043583A2 (en) | 2001-11-20 | 2003-05-30 | Seattle Genetics, Inc. | Treatment of immunological disorders using anti-cd30 antibodies |
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2000
- 2000-11-28 US US09/724,406 patent/US7090843B1/en not_active Expired - Lifetime
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2001
- 2001-11-28 AU AU3651802A patent/AU3651802A/xx active Pending
- 2001-11-28 DK DK01986050.1T patent/DK1347730T4/da active
- 2001-11-28 JP JP2002545640A patent/JP4303964B2/ja not_active Expired - Lifetime
- 2001-11-28 AU AU2002236518A patent/AU2002236518B2/en active Active
- 2001-11-28 AT AT01986050T patent/ATE454124T1/de active
- 2001-11-28 ES ES01986050T patent/ES2339333T5/es not_active Expired - Lifetime
- 2001-11-28 DE DE60141043T patent/DE60141043D1/de not_active Expired - Lifetime
- 2001-11-28 EP EP01986050.1A patent/EP1347730B2/en not_active Expired - Lifetime
- 2001-11-28 CA CA2430135A patent/CA2430135C/en not_active Expired - Lifetime
- 2001-11-28 WO PCT/US2001/044811 patent/WO2002043661A2/en not_active Ceased
- 2001-11-28 PT PT01986050T patent/PT1347730E/pt unknown
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2010
- 2010-01-29 CY CY20101100089T patent/CY1110700T1/el unknown
Also Published As
| Publication number | Publication date |
|---|---|
| EP1347730A2 (en) | 2003-10-01 |
| ES2339333T3 (es) | 2010-05-19 |
| EP1347730A4 (en) | 2005-08-17 |
| WO2002043661A3 (en) | 2003-01-16 |
| DK1347730T4 (da) | 2020-04-27 |
| EP1347730B2 (en) | 2013-05-29 |
| JP2005506035A (ja) | 2005-03-03 |
| AU3651802A (en) | 2002-06-11 |
| EP1347730B1 (en) | 2010-01-06 |
| ATE454124T1 (de) | 2010-01-15 |
| US7090843B1 (en) | 2006-08-15 |
| CA2430135A1 (en) | 2002-06-06 |
| AU2002236518B2 (en) | 2006-10-26 |
| CY1110700T1 (el) | 2015-06-10 |
| ES2339333T5 (es) | 2013-09-26 |
| DE60141043D1 (de) | 2010-02-25 |
| WO2002043661A2 (en) | 2002-06-06 |
| JP4303964B2 (ja) | 2009-07-29 |
| WO2002043661B1 (en) | 2003-03-06 |
| CA2430135C (en) | 2012-10-02 |
| DK1347730T3 (da) | 2010-02-01 |
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